Three scientists who helped to develop cryo-electron microscopy won the 2017 Nobel Prize in Chemistry. This is particularly relevant as the UM Life Sciences Institute has one of top Cryo-EM labs in the country! In this science video, two University of Michigan scientists from the field of Cryo-EM explain what it is, how it’s revolutionizing biology and how they are using it in their own labs.
Creating the Cryo-EM science video
Working again with Michigan Media, Kohlitz produced, shot b-roll and edited this science video highlighting an extraordinarily new science as used by two elite experts. Once the 2017 Nobel Prize in Chemistry was announced, the University of Michigan’s Life Sciences Institute realized it’s own distinct role in the news making subject and wanted to capitalize on the moment. With only about two weeks to produce, shoot and edit a video, Michigan Media and Kohlitz swept in, interviewed professors Melanie Ohi and Michael Cianfrocco, shot b-roll of some cool scinec-y things (liquid nitrogen anyone?) in one day, then Kohlitz edited a video in about 4 days. Maybe we’ll win a Nobel Prize in speed video someday.
Michael, “Cryo-EM is a technique for studying protein structure where we’ve frozen the protein in solution and then we image it in electron microscopes. And once we have all these images, we then can use computers to solve the structure.”
Melanie, “So, a structural biologist, what we really want to do is to get the 3D structures of these, so that we can see how they’re put together and how they work. For cyro-EM, we can purify the complex and we don’t have to make crystals, we can just look at it. So that’s a huge advantage and it allows us to look at complexes that are really dynamic, that are inserted in membranes, a lot of things that are more difficult for x-ray crystallography to do.”
Michael, “Cryo-EM has been recently recognized with a Nobel Prize in Chemistry.”
Melanie, “The people who won the Nobel Prize started understanding that theoretically using cryo-EM would allow them to determine atomic resolution structures.
Michael, “We now are able to take structures that were previously blobs and low resolution into much finer detail where we can see the individual amino acids in the protein.”
Melanie, “It took a revolution in technology development, which included better microscopes, better cameras and better computation.”
Michael, “And so cryo-EM requires us to analyze these large datasets using supercomputers that are collecting upwards of 10-20 terabytes — which is thousand of your iPhones — just for one dataset. But it turns out that getting access to theres types of high performance computing resources can be challenging for many labs, so part of what I’m trying to do right now is really remove the barrier to entry for these users, to let them solve their structures as fast as possible.”
Melanie, “The University of Michigan has been very forward-thinking and really invested in this technology. That means a lot. Becasue that means now we have a functioning facility with all this technology, where other people are now trying to buy it and get it set up.
Michael, “For me in my lab here at the Life Science Institute, we’re going to be using cryo-EM to study how motor proteins actually are able to recognize and move different parts of the cell all over the place. And so we’re trying to understand the structure of their proteins, and how that structure relates to both their normal function and how this function is misregulated in neurodegenerative diseases.”
Melanie, “So my lab focuses on the structure of bacterial toxins, and what we’re trying to do is figure out how a toxin is secreted as protein in solution and then can insert into the membrane and form a pore. And so really our goal is to help other scientists figure out how to stop these toxins from doing their job.”